Structural Basis of von Willebrand Factor Activation by the Snake Toxin Botrocetin

The A1 domain of von Willebrand factor (vWF) mediates platelet adhesion to sites of vascular injury by binding to the platelet receptor glycoprotein Ib (GpIb), an interaction that is regulated by hydrodynamic shear forces. The GpIb binding surface of A1 is distinct from a regulatory region, suggesti...

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Veröffentlicht in:	Structure (London) 2002-07, Vol.10 (7), p.943-950
Hauptverfasser:	Fukuda, Koichi, Doggett, Teresa A., Bankston, Laurie A., Cruz, Miguel A., Diacovo, Thomas G., Liddington, Robert C.
Format:	Artikel
Sprache:	eng
Schlagworte:	A1 domain activation Blood Platelets - drug effects Blood Platelets - physiology Cell Adhesion - drug effects Crotalid Venoms - chemistry Crotalid Venoms - pharmacology Crystallography, X-Ray gain-of-function Humans In Vitro Techniques Models, Molecular Mutation PARTICLE ACCELERATORS platelet adhesion Protein Conformation SNAKES STANFORD LINEAR ACCELERATOR CENTER STANFORD SYNCHROTRON RADIATION LABORATORY SYNCHROTRON RADIATION TOXINS von Willebrand factor von Willebrand Factor - chemistry von Willebrand Factor - genetics von Willebrand Factor - physiology
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